ID A0A091QRY4_MERNU Unreviewed; 742 AA.
AC A0A091QRY4;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=HECT-type E3 ubiquitin transferase {ECO:0000256|ARBA:ARBA00012485};
DE EC=2.3.2.26 {ECO:0000256|ARBA:ARBA00012485};
DE Flags: Fragment;
GN ORFNames=N331_04869 {ECO:0000313|EMBL:KFQ29948.1};
OS Merops nubicus (Northern carmine bee-eater).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Coraciiformes; Meropidae; Merops.
OX NCBI_TaxID=57421 {ECO:0000313|EMBL:KFQ29948.1, ECO:0000313|Proteomes:UP000052967};
RN [1] {ECO:0000313|EMBL:KFQ29948.1, ECO:0000313|Proteomes:UP000052967}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N331 {ECO:0000313|EMBL:KFQ29948.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine +
CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-
CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.;
CC EC=2.3.2.26; Evidence={ECO:0000256|ARBA:ARBA00000885};
CC -!- PATHWAY: Protein modification; protein ubiquitination.
CC {ECO:0000256|ARBA:ARBA00004906}.
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DR EMBL; KK705383; KFQ29948.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091QRY4; -.
DR UniPathway; UPA00143; -.
DR Proteomes; UP000052967; Unassembled WGS sequence.
DR GO; GO:0061630; F:ubiquitin protein ligase activity; IEA:InterPro.
DR GO; GO:0016567; P:protein ubiquitination; IEA:UniProtKB-UniPathway.
DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro.
DR CDD; cd08382; C2_Smurf-like; 1.
DR CDD; cd00078; HECTc; 1.
DR CDD; cd00201; WW; 3.
DR Gene3D; 2.20.70.10; -; 2.
DR Gene3D; 2.60.40.150; C2 domain; 1.
DR Gene3D; 3.30.2160.10; Hect, E3 ligase catalytic domain; 1.
DR Gene3D; 3.30.2410.10; Hect, E3 ligase catalytic domain; 1.
DR Gene3D; 3.90.1750.10; Hect, E3 ligase catalytic domains; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR024928; E3_ub_ligase_SMURF1.
DR InterPro; IPR000569; HECT_dom.
DR InterPro; IPR035983; Hect_E3_ubiquitin_ligase.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR PANTHER; PTHR11254:SF300; E3 UBIQUITIN-PROTEIN LIGASE SMURF2; 1.
DR PANTHER; PTHR11254; HECT DOMAIN UBIQUITIN-PROTEIN LIGASE; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF00632; HECT; 1.
DR Pfam; PF00397; WW; 3.
DR PIRSF; PIRSF001569; E3_ub_ligase_SMURF1; 3.
DR SMART; SM00239; C2; 1.
DR SMART; SM00119; HECTc; 1.
DR SMART; SM00456; WW; 3.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR SUPFAM; SSF56204; Hect, E3 ligase catalytic domain; 1.
DR SUPFAM; SSF51045; WW domain; 3.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS50237; HECT; 1.
DR PROSITE; PS01159; WW_DOMAIN_1; 1.
DR PROSITE; PS50020; WW_DOMAIN_2; 3.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000052967};
KW Ubl conjugation pathway {ECO:0000256|ARBA:ARBA00022786,
KW ECO:0000256|PROSITE-ProRule:PRU00104}.
FT DOMAIN 1..108
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 146..179
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 240..273
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 286..319
FT /note="WW"
FT /evidence="ECO:0000259|PROSITE:PS50020"
FT DOMAIN 408..742
FT /note="HECT"
FT /evidence="ECO:0000259|PROSITE:PS50237"
FT ACT_SITE 710
FT /note="Glycyl thioester intermediate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001569-1,
FT ECO:0000256|PROSITE-ProRule:PRU00104"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFQ29948.1"
FT NON_TER 742
FT /evidence="ECO:0000313|EMBL:KFQ29948.1"
SQ SEQUENCE 742 AA; 85621 MW; 1F355F5ADCBF271C CRC64;
ISVFLTVLCA KNLVKKDFFR LPDPFAKVVV DGSGQCHSTD TVKNTLDPKW NQHYDLYIGK
SDSITISVWN HKKIHKKQGA GFLGCVRLLS NAINRLKDTG YQRLDLCKLG PNDNDTVRGQ
IVVSLQSRDR IGTGGQVVDC SRLFDNDLPD GWEERRTASG RIQYLNHITR TTQWERPTRP
ASEYSSPGRP LSCFVDENTP ITGTNGATCG QTSDPRLAER RVRSQRHRNY MSRTHLHTPP
DLPEGYEQRT TQQGQVYFLH TQTGVSTWHD PRVPRDLSNI NCEELGPLPP GWEIRNTATG
RVYFVDHNNR TTQFTDPRLS ANLHLVLNRQ NQLKDQQHQQ QQQVVSLCQL PDEAECLTVP
RYKRDLVQKL KILRQELSQQ QPQAGHCRIE VSREEIFEES YRQVMKMRPK DLWKRLMIKF
RGEEGLDYGG VAREWLYLLS HEMLNPYYGL FQYSRDDIYT LQINPDSAVN PEHLSYFHFV
GRIMGMAVFH GHYIDGGFTL PFYKQLLGKP ITLDDMELVD PDLHNSLVWI LENDITGVLD
HTFCVEHNAY GEIIQHELKP NGKSIPVTEE NKKEYVRLYV NWRFLRGIEA QFLALQKGFN
EVIPQHLLKT FDEKELELII CGLGKIDVND WKANTRLKHC TPDSNIVKWF WKAVEFFDEE
RRARLLQFVT GSSRVPLQGF KALQGAAGPR LFTIHQIDAS TNNLPKAHTC FNRIDIPPYE
SYDKLYEKLL TAIEETCGFA VE
//
